Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2009 Oct;109(10):4760-79.
doi: 10.1021/cr900104z.

Structural biology of copper trafficking

Amie K Boal  1 , Amy C Rosenzweig
Affiliations
Review

Structural biology of copper trafficking

Amie K Boal et al. Chem Rev. 2009 Oct.
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1
Copper trafficking pathways in humans.
Figure 2
Figure 2
Overall architecture of hCtr1.
Figure 3
Figure 3
Overall architecture of Cu(I) P1B-type ATPases. The number of MBDs at the N-terminus ranges from one to six, depending on the organism.
Figure 4
Figure 4
Copper trafficking pathways in bacteria. CopA ATPases are found in both gram-positive and gram-negative (shown here) bacteria. A CopZ homolog is not found in E. coli, but is found in the gram-positive bacteria B. subtilis and E. hirae. The Pco (also known as Cop) and Cus systems are specific to gram-negative bacteria.
Figure 5
Figure 5
Copper trafficking pathways in the cyanobacterium Synechocystis PCC 6803.
Figure 6
Figure 6
Solution structure of Cu(I)-Atx1 (PDB accession code 1FD8). The Cu(I) ion is shown as a gray sphere and the two coordinating cysteine residues are shown as sticks.
Figure 7
Figure 7
Crystal structure of Cu(I)-Atox1 (PDB accession code 1FEE). The two monomers are shown in dark blue and cyan and the Cu(I) ion is shown as a gray sphere. Coordinating cysteine residues and adjacent lysine residues are shown as sticks.
Figure 8
Figure 8
Proposed mechanism of Cu(I) transfer between an Atx1-like chaperone and a N-terminal MBD of a Cu(I) P1B-type ATPase.
Figure 9
Figure 9
Solution structure of the second MBD of the Menkes disease protein (MNK2) (PDB accession code 1S6U). The Cu(I) ion is shown as a gray sphere and coordinating cysteine residues are shown as sticks. Residue Phe66 occupies the same position as the conserved lysine residue in the Atx1-like chaperones (Figure 6).
Figure 10
Figure 10
Solution structure of the fifth and sixth MBDs of the Wilson disease protein (WLN56) (PDB accession code 2EW9). The two CXXC motifs are shown as sticks.
Figure 11
Figure 11
Solution structure of the Wilson N domain (PDB accession code 2ARF). Invariant residues involved in ATP binding are highlighted. Residue His1069 is mutated in Wilson disease patients. The two asterisks denote the termini of an extended unstructured region.
Figure 12
Figure 12
Crystal structure of the ATP binding domain from A. fulgidus CopA (PDB accession code 2B8E). The ATP binds in a cleft between the N- and P-domains. The unstructured loop in the Wilson N-domain (Figure 11) is not present.
Figure 13
Figure 13
Crystal structure of the A domain from A. fulgidus CopA (PDB accession code 2HC8). The conserved GE sequence is highlighted.
Figure 14
Figure 14
Solution structure of the complex between Atx1 and Ccc2a (PDB accession code 2GGP). The Cu(I) ion is shown as a gray sphere and is coordinated by Cys15 from Atx1 and Cys13 and Cys16 from Ccc2a.
Figure 15
Figure 15
Crystal structure of P. syringae CopC at pH 7.5 (PDB accession code 2C9Q). The Cu(I) ion (gray sphere) is coordinated by His48 and Met40. The Cu(II) ion (cyan sphere) is coordinated by the N-terminal amino group, His1, His91, and a water molecule (red sphere).
Figure 16
Figure 16
Crystal structure of E. coli CusF (PDB accession code 2VB2). The Cu(I) ion (gray sphere) is coordinated by His36, Met47, and Met49, and interacts with Trp44 via a cation-π interaction.
Figure 17
Figure 17
Crystal structure of the complex between yCCS and ySOD1 (yellow) (PDB accession code 1JK9). Domain I of yCCS is shown in green, domain II is shown in blue, and domain III is shown in dark blue. The functionally important CXC motif in domain III is shown as sticks.
See this image and copyright information in PMC

References

    1. Crichton RR, Pierre J-L. Biometals. 2001;14:99. - PubMed
    1. da Silva J. J. R. Fraústo, Williams RJP. The biological chemistry of the elements. Second ed Oxford University Press; Oxford: 2001.
    1. Kaim W, Rall J. Angew. Chem. Int. Ed. Engl. 1996;35:43.
    1. Ochiai EI. J. Chem. Ed. 1986;63:942.
    1. Ridge PG, Zhang Y, Gladyshev VN. PLoS ONE. 2008;3:e1378. - PMC - PubMed

Publication types